Tyrosine Phosphorylation of Plakoglobin Causes Contrary Effects on Its Association with Desmosomes and Adherens Junction Components and Modulates β-Catenin-Mediated Transcription

@article{Miravet2003TyrosinePO,
  title={Tyrosine Phosphorylation of Plakoglobin Causes Contrary Effects on Its Association with Desmosomes and Adherens Junction Components and Modulates $\beta$-Catenin-Mediated Transcription},
  author={Susana Miravet and José A. Piedra and Julio Casta{\~n}o and Imma Raurell and Clara Francí and Mireia Du{\~n}ach and Antonio Garc{\'i}a de Herreros},
  journal={Molecular and Cellular Biology},
  year={2003},
  volume={23},
  pages={7391 - 7402}
}
ABSTRACT Plakoglobin is a protein closely related to β-catenin that links desmosomal cadherins to intermediate filaments. Plakoglobin can also substitute for β-catenin in adherens junctions, providing a connection between E-cadherin and α-catenin. Association of β-catenin with E-cadherin and α-catenin is regulated by phosphorylation of specific tyrosine residues; modification of β-catenin Tyr654 and Tyr142 decreases binding to E-cadherin and α-catenin, respectively. We show here that… 
Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes.
TLDR
Using purified proteins, it is shown that desmosomal cadherins and alpha-catenin compete directly for binding to plakoglobin, consistent with the absence of alpha- catenin in desmosomes.
β-Catenin and Plakoglobin N- and C-tails Determine Ligand Specificity*
TLDR
It is shown that, as reported for β-catenin, plakoglobin terminal tails also interact with the central domain and regulate the ability of this region to bind to different cofactors, contributing to the understanding of the molecular basis of the interactions established by these key regulators of epithelial tumorigenesis.
Presenilin-1 interacts with plakoglobin and enhances plakoglobin-Tcf-4 association. IMPLICATIONS FOR THE REGULATION OF β-CATENIN/Tcf-4-DEPENDENT TRANSCRIPTION.
TLDR
The effects of PS1 on the activity of this complex in epithelial cells are independent of its γ-secretase activity and its interaction with β-catenin, and PS1 association with plakoglobin enhances the interaction of this molecule with Tcf-4 and prevents its binding to DNA.
c-Src mediated tyrosine phosphorylation of plakophilin 3 as a new mechanism to control desmosome composition in cells exposed to oxidative stress
TLDR
It is discovered that reactive oxygen species (ROS) trigger the c-Src kinase-mediated tyrosine (Tyr)-195 phosphorylation of PKP3, which is identified as aosphorylation target of epidermal growth factor receptor signaling and occurs in certain poorly differentiated adenocarcinomas of the prostate, suggesting a possible role in tumor progression.
Gamma-Secretase-Dependent and -Independent Effects of Presenilin1 on β-Catenin·Tcf-4 Transcriptional Activity
TLDR
It is shown that in murine embryonic fibroblasts (MEFs) the mechanisms of action of the processed and non-processed forms of PS1 on β-catenin·Tcf-4 transcription are different, indicating that prevention of PS 1 processing in FAD affects the mechanism of repression of the transcriptional activity dependent onβ- catenin.
β-Catenin-Dependent and -Independent Effects of ΔN-Plakoglobin on Epidermal Growth and Differentiation
TLDR
The expression of ΔN122-PG in β-catenin-null skin significantly increased the survival rate of mutant mice, rescued differentiation, and limited excessive proliferation in the interfollicular epidermis, suggesting that plakoglobin may be involved in the intracellular signaling events essential for epidermal differentiation.
Mechanisms of Plakoglobin-dependent Adhesion
TLDR
Introduction of a phosphorylation-deficient PG mutant into PG null cells prevented the EGF receptor-dependent loss of desmoplakin from junctions, attenuating the effects of long term EGF treatment on cell adhesion.
Plakoglobin maintains the integrity of vascular endothelial cell junctions and regulates VEGF-induced phosphorylation of VE-cadherin
TLDR
It is indicated that plakoglobin plays multiple roles in regulation of cell-cell adhesion in a context dependent manner by inducing destabilization of the membrane distribution of VE-cadherin and resulted in increased permeability.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 53 REFERENCES
Tyrosine Phosphorylation of Human Keratinocyte β-Catenin and Plakoglobin Reversibly Regulates their Binding to E-Cadherin and α-Catenin
TLDR
The data raise the possibility that β-catenin or plakoglobin released from the adherens junctions by tyrosine phosphorylation may transduce a signal to the nucleus regarding the adhesive state of the cell.
Tyrosine-phosphorylated Plakoglobin Is Associated with Desmogleins but Not Desmoplakin after Epidermal Growth Factor Receptor Activation*
TLDR
Results are consistent with the possibility that EGF-dependent tyrosine phosphorylation of Pg may modulate cell-cell adhesion by compromising the link between desmosomal cadherins and the intermediate filament cytoskeleton.
p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate β-Catenin Tyr-142 Phosphorylation and β-Catenin-α-Catenin Interaction
TLDR
Results indicate that p120 catenin acts as a docking protein facilitating the activation of Fer/Fyn tyrosine kinases by Yes and demonstrate the role of these p 120 caten in-associated kinases in the regulation of β-catenin-α-catanin interaction.
Regulated binding of PTP1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of beta-catenin
TLDR
It is demonstrated that a PTP1B-like tyrosine phosphatase associates with N-cadherin and may function as a regulatory switch controlling cadherin function by dephosphorylating beta-catenin, thereby maintaining cells in an adhesion-competent state.
Regulation of E-cadherin/Catenin Association by Tyrosine Phosphorylation*
TLDR
Transient transfections of different mutants demonstrated that Tyr-654 is phosphorylated in conditions in which adherens junctions are disrupted and evidenced that binding ofβ-catenin to E-cadherin in vivo is controlled by phosphorylation of β- catenin Tyr-652.
Beta-catenin interacts with low-molecular-weight protein tyrosine phosphatase leading to cadherin-mediated cell-cell adhesion increase.
TLDR
It is proposed that the stability of cell-cell contacts at the adherens junction level is positively influenced by LMW-PTP expression, mainly because of the beta-catenin and LMW -PTP interaction at the plasma membrane level with consequent dephosphorylation.
The Transcriptional Factor Tcf-4 Contains Different Binding Sites for β-Catenin and Plakoglobin*
TLDR
It is shown here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58–Ser-59– Ser-60, and that simultaneous binding of the two armadillo proteins to TCF-4 is possible.
COMMENTARY Plakoglobin and β-catenin: protein interactions, regulation and biological roles
TLDR
Although plakoglobin differs from β catenin in its functions and is unable to compensate for defects in Wnt signaling resulting from lack of β-catenin, recent evidence suggests that plakoxide plays a unique role in WNT signaling that is different from that of βcaten in.
The amino- and carboxyl-terminal tails of (beta)-catenin reduce its affinity for desmoglein 2.
TLDR
It is proposed that a sequence in the first 26 amino acids of beta-catenin along with its carboxyl-terminal tail decrease its affinity for desmoglein and prevent its inclusion in the desmosome.
Plakoglobin and beta-catenin: protein interactions, regulation and biological roles.
TLDR
Although plakoglobin differs from beta- catenin in its functions and is unable to compensate for defects in Wnt signaling resulting from lack of beta-catenin, recent evidence suggests that plakoxide plays a unique role in WnT signaling that is different from that of Beta-Catenin.
...
1
2
3
4
5
...